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Title
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Crystal structure of a mammalian phosphoinositide-specific phospholipase C delta.
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Authors
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L.O.Essen,
O.Perisic,
R.Cheung,
M.Katan,
R.L.Williams.
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Ref.
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Nature, 1996,
380,
595-602.
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PubMed id
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Abstract
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Mammalian phosphoinositide-specific phospholipase C enzymes (PI-PLC) act as
signal transducers that generate two second messengers,
inositol-1,4,5-trisphosphate and diacylglycerol. The 2.4-A structure of
phospholipase C delta 1 reveals a multidomain protein incorporating modules
shared by many signalling proteins. The structure suggests a mechanism for
membrane attachment and Ca2+-dependent hydrolysis of second-messenger
precursors. The regulation and reversible membrane association of PI-PLC may
serve as a model for understanding other multidomain enzymes involved in
phospholipid signalling.
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